Table 1 Kinetic parameters of ALAS enzymes for ALA formationa.

From: Heme-dependent Inactivation of 5-Aminolevulinate Synthase from Caulobacter crescentus

ALASs

\({{\boldsymbol{K}}}_{{\boldsymbol{d}}}^{{\boldsymbol{Gly}},{\boldsymbol{app}}}\)

\({{\boldsymbol{K}}}_{{\boldsymbol{s}}}^{{\boldsymbol{Gly}}}\)

\({{\boldsymbol{K}}}_{{\boldsymbol{m}}}^{{\boldsymbol{Gly}}}\)

\({{\boldsymbol{K}}}_{{\boldsymbol{m}}}^{{\boldsymbol{SCoA}}}\)

k cat

mM

mM

mM

µM

s−1

C. crescentus

  Wild type

10.56 ± 1.35

12.45 ± 1.74

3.31 ± 0.45

2.42 ± 0.32

1.73 ± 0.09

  H340A

11.53 ± 1.17

15.02 ± 2.73

3.52 ± 0.67

2.40 ± 0.46

1.61 ± 0.12

  C398A

13.57 ± 3.10

15.63 ± 2.19

3.40 ± 0.47

2.55 ± 0.32

1.69 ± 0.07

  H340A/C398A

6.46 ± 1.50

12.85 ± 2.27

3.57 ± 0.58

2.58 ± 0.39

1.79 ± 0.10

human ALAS2b,c

—

2.1 ± 0.4

15 ± 3

4.3 ± 0.6

0.030 ± 0.002

murine ALAS2d

—

8.0 ± 0.1

25 ± 4

1.3 ± 0.9

0.14 ± 0.02

R. capsuatus e

—

—

0.25 ± 0.009

0.36 ± 0.14

0.27 ± 0.09

R. sphaeroides f,g

—

—

0.2e–1.9f

0.5e–17f

0.12

  1. aSee Supplementary Information for details about data analysis and parameters. Heme-bound form has no catalytic activity as shown in Fig. 2B.
  2. bDucamp, S., et al.25.
  3. cFratz, E. J., et al.26.
  4. dLendrihas, T., et al.27.
  5. eKaufholz, A. L., et al.16.
  6. fJordan, P. M. and A. Laghai-Newton28.
  7. gBolt, E. L., et al.29.
Back to article page